Robyn L. Stanfield mainly focuses on Antibody, Epitope, Virology, Stereochemistry and Glycoprotein. Her Antibody study frequently links to related topics such as Antigen. Her Epitope research integrates issues from Viral envelope, Molecular biology, Glycan, Protein structure and Binding site.
Her Glycan research includes themes of Gp41 and Crystal structure. The study incorporates disciplines such as Glycosylation and Immune system in addition to Virology. Her Stereochemistry research is multidisciplinary, incorporating perspectives in Peptide and Antibody antigen.
Her scientific interests lie mostly in Antibody, Virology, Epitope, Stereochemistry and Crystal structure. Robyn L. Stanfield has researched Antibody in several fields, including Molecular biology, Glycoprotein, Glycan and Antigen. Her Virology study combines topics in areas such as Immunogen and Immune system.
She combines subjects such as Protein structure, Biochemistry, Immunoglobulin Fab Fragments and Monoclonal antibody with her study of Epitope. Robyn L. Stanfield has included themes like Peptide sequence and Binding site in her Protein structure study. Her Stereochemistry research incorporates themes from Residue, Amino acid and Cyclic peptide, Peptide.
Robyn L. Stanfield spends much of her time researching Virology, Antibody, Zinc finger, DNA-binding domain and DNA. Her work deals with themes such as Anti hiv 1, Glycoprotein and Immunogenicity, which intersect with Virology. Her Antibody research is multidisciplinary, incorporating elements of Antigen and Glycan.
Her research in Zinc finger intersects with topics in Computational biology and Stereochemistry. Her Stereochemistry study combines topics from a wide range of disciplines, such as Kinase and Peptide. Robyn L. Stanfield studied DNA and Binding site that intersect with Molecular biology and Protein dynamics.
The scientist’s investigation covers issues in Antibody, Virology, Epitope, Glycoprotein and Glycan. Her work on Monoclonal and Immunoglobulin light chain as part of general Antibody study is frequently linked to Fluorescence anisotropy and Proteotoxicity, therefore connecting diverse disciplines of science. When carried out as part of a general Virology research project, her work on Neutralization is frequently linked to work in Glycopeptide, therefore connecting diverse disciplines of study.
Her research integrates issues of Junctional diversity, Ebola virus, Heptad repeat and Antibody Repertoire in her study of Epitope. Her work in Glycoprotein tackles topics such as Hepatitis C virus which are related to areas like Receptor and Gene family. Her studies in Glycan integrate themes in fields like Protein structure, Plasma protein binding, Immunogen and Furin.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
An alphabeta T cell receptor structure at 2.5 A and its orientation in the TCR-MHC complex.
K.C Garcia;M Degano;R.L Stanfield;A Brunmark.
Science (1996)
How TCRs Bind MHCs, Peptides, and Coreceptors
Markus G. Rudolph;Robyn L. Stanfield;Ian A. Wilson.
Annual Review of Immunology (2006)
Crystal structure of a neutralizing human IGG against HIV-1: a template for vaccine design.
Erica Ollmann Saphire;Paul W. H. I. Parren;Ralph Pantophlet;Michael B. Zwick.
Science (2001)
Structure of a V3-Containing HIV-1 gp120 Core
Chih-chin Huang;Min Tang;Mei-Yun Zhang;Shahzad Majeed.
Science (2005)
Antibody Domain Exchange Is an Immunological Solution to Carbohydrate Cluster Recognition
Daniel A. Calarese;Christopher N. Scanlan;Michael B. Zwick;Songpon Deechongkit.
Science (2003)
The Broadly Neutralizing Anti-Human Immunodeficiency Virus Type 1 Antibody 2G12 Recognizes a Cluster of α1→2 Mannose Residues on the Outer Face of gp120
Christopher N. Scanlan;Ralph Pantophlet;Mark R. Wormald;Erica Ollmann Saphire.
Journal of Virology (2002)
Crystal structure of a soluble cleaved HIV-1 envelope trimer.
Jean-Philippe Julien;Albert Cupo;Devin Sok;Devin Sok;Robyn L. Stanfield;Robyn L. Stanfield.
Science (2013)
A Potent and Broad Neutralizing Antibody Recognizes and Penetrates the HIV Glycan Shield
Robert Pejchal;Katie J. Doores;Katie J. Doores;Laura M. Walker;Reza Khayat.
Science (2011)
Antibody-antigen interactions: new structures and new conformational changes
Ian A. Wilson;Robyn L. Stanfield.
Current Opinion in Structural Biology (1994)
Broadly Neutralizing Anti-HIV Antibody 4E10 Recognizes a Helical Conformation of a Highly Conserved Fusion-Associated Motif in gp41
Rosa M.F. Cardoso;Michael B. Zwick;Robyn L. Stanfield;Renate Kunert.
Immunity (2005)
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